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ENZYME

ENZYME entry: EC 2.7.11.12

Accepted Name
cGMP-dependent protein kinase
Alternative Name(s)
3':5'-cyclic GMP-dependent protein kinase
cGMP-dependent protein kinase Ibeta
guanosine 3':5'-cyclic monophosphate-dependent protein kinase
PKG
PKG 1alpha
PKG 1beta
PKG II
Reaction catalysed
  • ATP + L-seryl-[protein] <=> ADP + H(+) + O-phospho-L-seryl-[protein]
  • ATP + L-threonyl-[protein] <=> ADP + H(+) + O-phospho-L-threonyl-[protein]
Comment(s)
  • cGMP is required to activate this enzyme.
  • The enzyme occurs as a dimer in higher eukaryotes.
  • The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites.
  • This domain catalyzes the phosphorylation by ATP to specific serine or threonine residues in protein substrates.
  • The enzyme also has two allosteric cGMP-binding sites (sites A and B).
  • Binding of cGMP causes a conformational change that is associated with activation of the kinase.
  • Formerly EC 2.7.1.37.
Cross-references
BRENDA2.7.11.12
EC2PDB2.7.11.12
ExplorEnz2.7.11.12
PRIAM enzyme-specific profiles2.7.11.12
KEGG Ligand Database for Enzyme Nomenclature2.7.11.12
IUBMB Enzyme Nomenclature2.7.11.12
IntEnz2.7.11.12
MEDLINEFind literature relating to 2.7.11.12
MetaCyc2.7.11.12
Rhea expert-curated reactions2.7.11.12
UniProtKB/Swiss-Prot
A8X6H1, EGL4_CAEBRO76360, EGL4_CAEELP00516, KGP1_BOVIN
Q03042, KGP1_DROMEQ13976, KGP1_HUMANP0C605, KGP1_MOUSE
O77676, KGP1_RABITQ03043, KGP24_DROMEP32023, KGP25_DROME
Q13237, KGP2_HUMANQ61410, KGP2_MOUSEQ64595, KGP2_RAT
Q8MMZ8, KGP_EIMTEA0A509AKL0, KGP_PLABAQ8I719, KGP_PLAF7
W7JX98, KGP_PLAFOA5K0N4, KGP_PLAVSQ8MMZ7, KGP_TOXGO

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